The objective of the overall research in this laboratory is centered on achieving as complete a description as possible for the structures of peptides, proteins, nucleic acids and their complexes in solution, principally by NMR spectroscopy. At present particular emphasis is being placed on developing approaches which allow the investigation of larger and complex systems as well as increase the precision which these solution structures can be obtained, studies aimed at correlating structure and function, and experiments aimed at investigating protein folding. Structures for several proteins have been determined and analyzed. These include the cytokine interleukin-4, and the complex of the DNA binding domain of the erythroid transcription factor GATA-1 with its specific DNA target site. These studies have exploited many novel 3D and 4D heteronuclear NMR experiments to dramatically increase spectral resolution and thereby resolve assignment ambiguities in larger proteins. The dynamics of the cytokine interleukin-8 have been explored. The contact surface of the IgG binding domain of Streptococcal G complexed with a human IgGFc has been identified. Finally, the folding pathway and kinetics of the all beta- sheet protein interleukin-1beta have been investigated.